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Literature summary for 7.1.2.2 extracted from

  • Wagner, K.; Rehling, P.; Sanjuan Szklarz, L.K.; Taylor, R.D.; Pfanner, N.; van der Laan, M.
    Mitochondrial F1Fo-ATP synthase: the small subunits e and g associate with monomeric complexes to trigger dimerization (2009), J. Mol. Biol., 392, 855-861.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane the enzyme is found in monomeric, dimeric and higher oligomeric forms in the inner mitochondrial membrane. Two small proteins of the membrane-embedded Fo-domain subunits e and g are dimer-specific subunits of yeast ATP synthase and are required for stabilization of the dimers Saccharomyces cerevisiae 5743
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Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Saccharomyces cerevisiae
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ADP + phosphate + H+/out
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r

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
Saccharomyces cerevisiae ADP + phosphate + H+/out
-
r

Subunits

Subunits Comment Organism
More the enzyme is found in monomeric, dimeric and higher oligomeric forms in the inner mitochondrial membrane. Dimerization of ATP synthase complexes is a prerequisite for the generation of larger oligomers that promote membrane bending and formation of tubular cristae membranes. Two small proteins of the membrane-embedded Fo-domain subunits e and g are dimer-specific subunits of yeast ATP synthase and are required for stabilization of the dimers. Subunits e and g sequentially assemble with monomeric ATP synthase to form a dimerization-competent primed monomer, overview Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
ATP synthase
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Saccharomyces cerevisiae
mitochondrial F1Fo-ATP synthase
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Saccharomyces cerevisiae